We wish to establish the nature of the enzymatic reactions involved in the aerobic degradation of L-beta-lysine by Pseudomonas B4 and of L-erythro-3,5-diaminohexanoate by Brevibacterium L5. In beta-lysine degradation we plan specifically to identify the reactions and characterize the enzymes responsible for the conversion of 3-keto-6-acetamidohexanoate (KAAH) to known metabolites. Optimal conditions for KAAH decomposition and product accumulation will be established. 14C-labeled KAAH will be used and 14C-labeled products will be separated by physical methods and identified. Specific radiochemical or chemical assays will be used in the isolation of novel enzymes by the usual methods of enzymology, and general properties of the enzymes will be determined. In 3,5-diaminohexanoate degradation, we plan specifically to look for the presence of 3-keto-5-aminohexanoate cleavage enzyme and 3-aminobutyryl-CoA deaminase. If present, we shall purify these enzymes and compare their properties with those of the corresponding clostridial enzymes. If absent, we shall look for alternative enzymes responsible for the decomposition of 3-keto-5-aminohexanoate.